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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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27565 | Chemical Shifts: 1 set |
Transmembrane protein 106B (TEM106B) |
TMEM106B, a risk factor for FTLD and aging, has an intrinsically disordered cytoplasmic domain
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Jian Kang, Jianxing Song, Liang Zhong Lim |
30389 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Solution structure of AGL55 |
Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization
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Cunjia Qiu, Francis J Castellino, Jaroslav Zajicek, Rashna D Balsara, Shaun W Lee, Teresa Brito-Robionson, Victoria A Ploplis, Yue Yuan, Zhong Liang |
30390 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
Solution structure of KTI55 |
Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization
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Cunjia Qiu, Francis J Castellino, Jaroslav Zajicek, Rashna D Balsara, Shaun W Lee, Teresa Brito-Robionson, Victoria A Ploplis, Yue Yuan, Zhong Liang |
36112 | Chemical Shifts: 1 set |
NMR structure of the domain 5 of the E. coli ribosomal protein S1 |
Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle
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Cynthia Y He, Jianxing Song, Jing Fu, Liang Zhong Z Lim, Shermaine Ee, Yanming Tan |
25595 | Chemical Shifts: 1 set |
NMR Structure of TDP-43 prion-like hydrophobic helix in DPC |
ALS-causing mutations significantly perturb the self-assembly and interaction with nucleic acid of the intrinsically-disordered prion-like domain of TDP-43
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Jianxing Song, Liang Zhong Lim |